ADAM10: Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth- like factor, ephrin-A2 and for constitutive and regulated alpha- secretase cleavage of amyloid precursor protein (APP). Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis. Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form. Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B. May regulate the EFNA5-EPHA3 signaling.
Protein type: Vesicle; Cell surface; Membrane protein, integral; Cell adhesion; Protease; EC 3.4.24.81; Motility/polarity/chemotaxis
Chromosomal Location of Human Ortholog: 15q22
Cellular Component: cell surface; cytoplasm; focal adhesion; Golgi apparatus; Golgi-associated vesicle; integral to membrane; intracellular membrane-bound organelle; membrane; nucleus; plasma membrane; postsynaptic density; trans-Golgi network
Molecular Function: endopeptidase activity; integrin binding; metalloendopeptidase activity; metallopeptidase activity; protein binding; protein homodimerization activity; protein kinase binding; receptor binding; SH3 domain binding; zinc ion binding
Biological Process: axon guidance; cell-cell signaling; collagen catabolic process; constitutive protein ectodomain proteolysis; ephrin receptor signaling pathway; epidermal growth factor receptor signaling pathway; extracellular matrix disassembly; extracellular matrix organization and biogenesis; in utero embryonic development; integrin-mediated signaling pathway; membrane protein ectodomain proteolysis; monocyte activation; negative regulation of cell adhesion; Notch receptor processing; Notch signaling pathway; PMA-inducible membrane protein ectodomain proteolysis; positive regulation of cell growth; positive regulation of cell migration; positive regulation of cell proliferation; protein amino acid phosphorylation; protein processing
Disease: Alzheimer Disease 18; Reticulate Acropigmentation Of Kitamura
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